The role of carbohydrate in determining the immunochemical properties of the hemagglutinin of influenza A virus.
Most of the carbohydrate was removed from influenza virus MRC II (H3N2) and its purified hemagglutinin (HA) on treatment with glycosidases, including alpha-mannosidase, beta-N-acetylglucosaminidase, beta-galactosidase and alpha-fucosidase. The release of 50 per cent of the carbohydrate from intact virus particles significantly affected hemagglutinating activity. The ability of untreated and glycosidase-treated virus to inhibit the binding of antibodies directed against the hemagglutinin was almost indistinguishable by competitive radioimmunoassay (RIA). Up to 60 per cent of the carbohydrate from the purified HA of influenza virus could be removed. The antigenicity of glycosidase treated HA molecules decreased 8-fold compared to intact HAs as measured by competitive RIA. In addition, glycosidase digestion of 125I-labeled HA resulted in a decrease in its reactivity in direct RIA. We conclude that the carbohydrate portion of the HA of influenza virus is not of major importance in defining the antigenicity of HA.
D000118:Acetylglucosaminidase / Q000494:pharmacology; D002241:Carbohydrates / Q000276:immunology*; D006389:Hemagglutinins, Viral / Q000276:immunology*; D009980:Influenza A virus / Q000276:immunology*; D008361:Mannosidases / Q000494:pharmacology; D005644:alpha-L-Fucosidase / Q000494:pharmacology; D043323:alpha-Mannosidase; D001616:beta-Galactosidase / Q000494:pharmacology
D002241:Carbohydrates; D006389:Hemagglutinins, Viral; D008361:Mannosidases; D001616:beta-Galactosidase; D043323:alpha-Mannosidase; D005644:alpha-L-Fucosidase; D000118:Acetylglucosaminidase